Results 71 to 80 of about 18,104 (240)

CRM1-mediated Recycling of Snurportin 1 to the Cytoplasm [PDF]

open access: yesThe Journal of Cell Biology, 1999
Importin β is a major mediator of import into the cell nucleus. Importin β binds cargo molecules either directly or via two types of adapter molecules, importin α, for import of proteins with a classical nuclear localization signal (NLS), or snurportin 1, for import of m3G-capped U snRNPs.
Paraskeva, E.   +7 more
openaire   +4 more sources

Rrp12 and the Exportin Crm1 Participate in Late Assembly Events in the Nucleolus during 40S Ribosomal Subunit Biogenesis [PDF]

open access: yes, 2016
This is an open-access article distributed under the terms of the Creative Commons Attribution License.During the biogenesis of small ribosomal subunits in eukaryotes, the pre-40S particles formed in the nucleolus are rapidly transported to the cytoplasm.
Dosil, Mercedes   +2 more
core   +1 more source

Recognition of nuclear export signals by CRM1 carrying the oncogenic E571K mutation

open access: yesMolecular Biology of the Cell, 2020
The E571K mutation of CRM1 is highly prevalent in some cancers, but its mechanism of tumorigenesis is unclear. Glu571 of CRM1 is located in its nuclear export signal (NES)-binding groove, suggesting that binding of select NESs may be altered.
J. Baumhardt   +7 more
semanticscholar   +1 more source

Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance

open access: yesAging and Cancer, EarlyView.
NPM1 mutations drive acute myeloid leukemia by acting as neomorphic transcriptional regulators that cooperate with Menin–MLL and XPO1 to sustain HOX/MEIS1 expression and block differentiation. Targeting these mutant‐specific transcriptional dependencies provides a rational therapeutic strategy for NPM1‐mutated AML.
Yanan Jiang   +3 more
wiley   +1 more source

Mechanisms Underlying the Delayed Activation of the Cap1 Transcription Factor in Candida albicans following Combinatorial Oxidative and Cationic Stress Important for Phagocytic Potency [PDF]

open access: yes, 2016
ACKNOWLEDGMENTS We are grateful to Brian Morgan and Elizabeth Veal for insightful discussions, Mélanie Ikeh for experimental assistance, and Scott Moye-Rowley (University of Iowa) for the gift of the anti-Cap1 antibody.
Brown, Alistair James Petersen   +8 more
core   +4 more sources

NXF1 and CRM1 nuclear export pathways orchestrate nuclear export, translation and packaging of murine leukaemia retrovirus unspliced RNA

open access: yesRNA Biology, 2020
Cellular mRNAs are exported from the nucleus as fully spliced RNAs. Proofreading mechanisms eliminate unprocessed and irregular pre-mRNAs to control the quality of gene expression.
M. Mougel   +6 more
semanticscholar   +1 more source

Role of SoxE transcription factors in development and disease

open access: yesDevelopmental Dynamics, EarlyView.
Abstract Sox8, Sox9, and Sox10 arose by multiple rounds of genome duplications from a single SoxE gene in ancestral vertebrates. In this review, we will briefly discuss the molecular structure and function of SoxE transcription factors and their evolutionary origin. We will then discuss their expression, function, and developmental disorders.
Merin Lawrence, Gerhard Schlosser
wiley   +1 more source

Putative Reaction Intermediates in Crm1-mediated Nuclear Protein Export [PDF]

open access: yesJournal of Biological Chemistry, 1999
We discovered several novel interactions between proteins involved in Crm1-mediated nuclear export of the nuclear export signal containing human immunodeficiency virus type 1 protein Rev. First, a Rev/Crm1/RanGTP complex (where Ran is Ras-related nuclear protein) reacts with some nucleoporins (Nup42 and Nup159) but not others (NSP1, Nup116, and Nup1 ...
M, Floer, G, Blobel
openaire   +2 more sources

Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.

open access: yesPLoS ONE, 2011
Proteins bearing a leucine-rich nuclear export signal (NES) are exported from the nucleus by the transport factor CRM1, which forms a cooperative ternary complex with the NES-bearing cargo and with the small GTPase Ran.
Karla Langer   +4 more
doaj   +1 more source

Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr [PDF]

open access: yes, 2009
Background Tpr is a large protein with an extended coiled-coil domain that is localized within the nuclear basket of the nuclear pore complex. Previous studies 1 involving antibody microinjection into mammalian cells suggested a role for Tpr in nuclear ...
Iris Ben-Efraim   +2 more
core   +2 more sources

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